期刊
MOLECULAR NUTRITION & FOOD RESEARCH
卷 51, 期 9, 页码 1107-1110出版社
WILEY
DOI: 10.1002/mnfr.200700017
关键词
disease; glyeation; glyoxalase; receptor; S100 proteins
资金
- BBSRC [BB/D006295/2] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D006295/2] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
The receptor for advanced glycation endproducts (RAGE) has a well-substantiated role in cell dysfunction and mechanisms of inflammatory disease. The physiological agonists of RAGE are less certain: S100/calgranulin proteins, high mobility group-1 protein HMGB1 and other proteins are candidate agonists. It increasingly appears unlikely proteins modified by advanced glycation endproducts are effective agonists in vivo. In the following debate, Professors Ann Marie Schmidt and Claus Heizmann gave arguments and evidences for and against the motion. Recent evidence suggesting the activation of RAGE impairs the enzymatic defence against glycation provided by glyoxalase 1 (Glo 1) suggests that studies of RAGE will continue to be of importance to our understanding of the physiological significance of protein glycation.
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